ID J9RIT5_9ACTN Unreviewed; 1129 AA.
AC J9RIT5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN ORFNames=KTR9_1743 {ECO:0000313|EMBL:AFR48382.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR48382.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR48382.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR48382.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC carboxylation of the covalently attached biotin in the first step and
CC the transfer of the carboxyl group to pyruvate in the second.
CC {ECO:0000256|PIRNR:PIRNR001594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953,
CC ECO:0000256|PIRNR:PIRNR001594};
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DR EMBL; CP002907; AFR48382.1; -; Genomic_DNA.
DR RefSeq; WP_014926253.1; NC_018581.1.
DR AlphaFoldDB; J9RIT5; -.
DR STRING; 337191.KTR9_1743; -.
DR KEGG; gor:KTR9_1743; -.
DR PATRIC; fig|337191.3.peg.2014; -.
DR eggNOG; COG1038; Bacteria.
DR HOGENOM; CLU_000395_0_0_11; -.
DR Proteomes; UP000003281; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01235; pyruv_carbox; 1.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594};
KW Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:AFR48382.1}.
FT DOMAIN 1..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 526..795
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1055..1129
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 535
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 607
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 705
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 734
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 736
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 869
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 705
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1095
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1129 AA; 120929 MW; 749F0BEBEDE005DA CRC64;
MFDKVLVANR GEIAIRAFRA AYELGARTVA IFPYEDRTSV HRLKADESYQ IGVPGHPVRA
YLSVDEVVSA AVRCGADAIY PGYGFLSENQ GLAAACAEAG ITFVGPSADI LEMTGNKATA
VAAAKAAGIP VLASSEPSSD LDELLAAAED MQFPVFVKAV AGGGGRGMRR VDERADLAEA
IAAASREAEA AFGDATVFLE QAVVNPRHIE VQILADTYGN VIHLYERDCS LQRRHQKVIE
LAPAPNLSDE LRERICSDAV AFARSIGYSC AGTVEFLLDE QGRHVFIEMN PRIQVEHTVT
EEITDVDLVS AQLRIASGES LADLGLSQDV IGIRGAALQC RITTEDPANG FRPDVGRITA
YRSPGGAGVR LDGGATLGAE VSGHFDSMLV KLTCRGRDFP TAMRRARRAV AEFRIRGVAT
NIPFLQAVLD DPDFRAGRVT TSFIDERPGL LTSRSSADRG TKILSYLADV TVNKPHGERP
TTVYPRDKLP TVERSVLASP PNGSRQRLLE LGPEGFARDL RENPRLGITD TTFRDAHQSL
LATRVRTNGL LNVAPYVAAL TPELLSVECW GGATYDVALR FLKEDPWDRL AQLREAIPNI
CLQMLLRGAN TVGYTPYPTK VTTAFVSEAT DVGIDIFRIF DALNNIDAMR PAIDAVRETG
TAVAEVAMSY TGDLSDPAED LYTLDYYLRL AEQIVEAGAH VLAIKDMAGL LRAPAATTLV
TALRREFDLP IHVHTHDTPG GQLATYMAAW QAGADAVDGA SAALAGTTSQ PPLSAIVAAT
AHTERDSGID LARVCDLEPY WEALRKVYSP FESGLPAPTG RVYSHEIPGG QLSNLRQQAI
SLGLGNRFEA VEQAYAAADS MLGRLVKVTP SSKVVGDLAL ALVGRGITAS DFAADPASYD
IPDSVIGFLR GELGDPPGGW PEPLRTLALQ GRAPAPEVTE LTADDEAILD KPGRDRQVRL
NHLLFPGPAK EFEEHYEAYG DTSTLSANQF FYGLRYGEEH RVVLEPGVDL LIGLEAISEP
DEQGMRTVMC VLNGQLRPIA VRDHSVDSAV ASAEKADRSD PHHIGAPFAG VVSLSVDVGD
EVAVGATIGT IEAMKMEAAI TAPVAGKVAR LAVGQVTQVA PGDLLIEIR
//
